نتائج البحث

1

Mutations in myosin S2 alter cardiac myosin-binding protein-C interaction in hypertrophic cardiomyopathy in a phosphorylation-dependent manner

المؤلفون: Sakthivel Sadayappan, James W. McNamara, Rohit R. Singh

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, hC0-C2, human C0-C2, HCM, hypertrophic cardiomyopathy, S2, subfragment 2 region, 126 amino acids of myosin, Mutant, Biochemistry, SPBA, solid-phase binding assay, MYBPC3, MYH7, hS2, human cardiac myosin S2, hC0-C2p, phosphorylation of hC0-C2, Myosin, Phosphorylation, hS2E930Δ, human recombinant proximal S2 protein with E930Δ mutation, chemistry.chemical_classification, Chemistry, Cardiac muscle, Hypertrophic cardiomyopathy, cMyBP-C, cardiac myosin-binding protein-C, Cell biology, Amino acid, myosin S2, medicine.anatomical_structure, Kd, dissociation constant, Research Article, hS2Wt, human recombinant proximal S2 WT protein, Protein Binding, DRX, disordered relaxed state, Bmax, maximal binding capacity, ktr, rate of force redevelopment, Mice, Transgenic, macromolecular substances, Myosins, 03 medical and health sciences, MYBPC3, human cardiac myosin-binding protein-C gene, AAA, phospho-ablated cMyBP-C or phospho-ablation, medicine, Animals, Humans, β-MyHC, β-myosin heavy chain, η, stoichiometry, MYH7, β-myosin heavy-chain gene, Molecular Biology, 4LP, four-parameter logistic curve, SRX, super-relaxed, mC0-C2, mouse recombinant C0-C2 protein, 030102 biochemistry & molecular biology, Binding protein, β-AR, β-adrenergic receptor, Reproducibility of Results, Cell Biology, S1, head of myosin, Cardiomyopathy, Hypertrophic, medicine.disease, ITC, isothermal titrating calorimetry, hS2R870H, human recombinant proximal S2 protein with R870H mutation, Kinetics, 030104 developmental biology, hS2E924K, human recombinant proximal S2 protein with E924K mutation, Mutation, Cattle, Mutant Proteins, Carrier Proteins, Peptides, DDD, phospho-mimetic cMyBP-C

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a57bd0689575396e21618a24f3574223Test
http://europepmc.org/articles/PMC8239744Test

2

Adaptation induced by self-targeting in a type I-B CRISPR-Cas system

المؤلفون: Uri Gophna, Israela Turgeman-Grott, Rachel Smith, Anita Marchfelder, Aris-Edda Stachler, Julia Wörtz, Rolf Backofen, Omer S. Alkhnbashi, Thorsten Allers

المصدر: The Journal of Biological Chemistry

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a0110889f04d45138ac079ea9555d69Test
http://europepmc.org/articles/PMC7521656Test

3

Enhanced accessibility and hydrophobicity of amyloidogenic intermediates of the β2-microglobulin D76N mutant revealed by high-pressure experiments

المؤلفون: Kazumasa Sakurai, Ryosuke Tomiyama

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Protein Folding, Amyloid, Mutant, Biochemistry, Anilino Naphthalenesulfonates, β2m, β2-microglobulin, 03 medical and health sciences, Protein Aggregates, ANS, 1-anilino-8-naphthalene sulfonate, Renal Dialysis, biophysics, Native state, Pressure, Humans, mutant, high-pressure experiment, Molecular Biology, β2-microglobulin, 030102 biochemistry & molecular biology, Beta-2 microglobulin, Chemistry, Tryptophan, Wild type, amyloid, Cell Biology, Amyloidosis, MD, molecular dynamics, MSA, molecular surface areas, Folding (chemistry), Kinetics, 030104 developmental biology, Biophysics, Protein folding, <ν>, center of the spectral mass, Mutant Proteins, fluorescence, beta 2-Microglobulin, Research Article, Signal Transduction

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4912a98335606e45ffef11f5058d328Test
http://europepmc.org/articles/PMC7950326Test

4

The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking

المؤلفون: Hiroaki Matsunami, Ikuroh Ohsawa, Kentaro Ikegami, Ryosuke Inoue, Yosuke Fukutani, Shuto Sakashita, Masafumi Yohda, Tomoyo Koshizawa, Ryohei Tamaki

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Dimer, membrane transport, Cell, Mutant, odorant receptors, Receptors, Odorant, Biochemistry, law.invention, Receptors, G-Protein-Coupled, 03 medical and health sciences, chemistry.chemical_compound, Mice, law, Cell Movement, medicine, Animals, Humans, Luciferase, G-protein–coupled receptor (GPCR), Receptor, Molecular Biology, chemistry.chemical_classification, dimerization, 030102 biochemistry & molecular biology, Chemistry, flow cytometry, Membrane Transport Proteins, Cell Biology, receptor-transporting protein, Membrane transport, molecular chaperone, Cell biology, Amino acid, Protein Transport, 030104 developmental biology, medicine.anatomical_structure, HEK293 Cells, Protein Structure and Folding, Odorants, Recombinant DNA, Molecular Chaperones

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54f23a47a8e283a07d925fbd58d6328fTest
http://europepmc.org/articles/PMC6779431Test

5

Identification of a druggable protein–protein interaction site between mutant p53 and its stabilizing chaperone DNAJA1

المؤلفون: Rama K. Mishra, Dandan Xu, Ryan Jones, Leyu Sun, Gary E. Schiltz, Xin Tong, Jie Liao, Guang Yu Yang

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Cyclin-Dependent Kinase Inhibitor p21, Mutant, DNAJA1, pancreatic cancer, Druggability, protein–protein docking, Mutation, Missense, DMSO, dimethyl sulfoxide, Biochemistry, Protein–protein interaction, 03 medical and health sciences, Mice, FBS, fetal bovine serum, Cell Line, Tumor, interacting pocket, wtp53, wildtype p53, Hsp, heat shock protein, WT, wildtype, Animals, Humans, Homology modeling, homology model, Molecular Biology, CHIP, C terminus of Hsc70-interacting protein, KO, knockout, 030102 biochemistry & molecular biology, biology, Chemistry, Protein Stability, mutant p53, mutp53, mutant p53, Wild type, Cell Biology, Editors' Pick, HSP40 Heat-Shock Proteins, Small molecule, Cell biology, 030104 developmental biology, Amino Acid Substitution, Gene Expression Regulation, in silico, Chaperone (protein), biology.protein, DNAJA1, DnaJ homolog subfamily A member 1, Small molecule binding, Tumor Suppressor Protein p53, Research Article

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d3f6e1d9d82b22ad12b655cfb8a1007Test
http://europepmc.org/articles/PMC7948449Test

6

Structural basis of KdpD histidine kinase binding to the second messenger c-di-AMP

المؤلفون: Mona Batish, Vijay Parashar, Anirudha Dutta

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, crystal structure, Staphylococcus aureus, Subfamily, Histidine Kinase, Protein Conformation, Mutant, methicillin-resistant Staphylococcus aureus, Crystallography, X-Ray, Biochemistry, Second Messenger Systems, 03 medical and health sciences, Bacterial Proteins, Protein Domains, Cyclic AMP, Humans, Molecular Biology, bacterial signal transduction, Histidine, 030102 biochemistry & molecular biology, Chemistry, Kinase, Histidine kinase, Walker motifs, Cell Biology, Staphylococcal Infections, Ligand (biochemistry), c-di-AMP, 030104 developmental biology, second messenger, Second messenger system, osmoregulation, Protein Kinases, Research Article

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8f820f267bff537a7073529030c8a3Test
http://europepmc.org/articles/PMC8214093Test

7

Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 β-lactamase

المؤلفون: Timothy Palzkill, Ian M. Furey, Liya Hu, B. V. Venkataram Prasad, Banumathi Sankaran, Shrenik C. Mehta

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Carbapenem, antibiotic resistance, MIC, minimum inhibitory concentration, Stereochemistry, Protein Conformation, medicine.medical_treatment, Mutant, Crystallography, X-Ray, Biochemistry, antibiotics, beta-Lactamases, 03 medical and health sciences, carbapenemase, Bacterial Proteins, enzyme kinetics, Catalytic Domain, medicine, polycyclic compounds, Humans, Enzyme kinetics, Molecular Biology, chemistry.chemical_classification, 030102 biochemistry & molecular biology, biology, Hydrolysis, CRE, carbapenem-resistant Enterobacteriaceae, Substrate (chemistry), Active site, Cell Biology, biochemical phenomena, metabolism, and nutrition, bacterial infections and mycoses, Enzyme structure, enzyme structure, Anti-Bacterial Agents, Klebsiella Infections, enzyme, Klebsiella pneumoniae, 030104 developmental biology, Enzyme, chemistry, Carbapenems, KPC-2, Klebsiella pneumoniae carbapenemase-2, Beta-lactamase, biology.protein, beta-lactamase, medicine.drug, Research Article

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba108f6f41c36e7ea785373a40db5e53Test
http://europepmc.org/articles/PMC8189571Test

8

DUSP7 regulates the activity of ERK2 to promote proper chromosome alignment during cell division

المؤلفون: Robert Damoiseaux, Yenni A Garcia, Bobby Tofig, Ivan Ramirez, Erick F. Velasquez, Xiao Guo, Jorge Z. Torres, Whitaker Cohn, Ankur A. Gholkar, Julian P. Whitelegge

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, cell division, WT, wild type, Accelerated Communication, Cell division, Mutant, Aneuploidy, Biochemistry, Medical and Health Sciences, environment and public health, Chromosome segregation, NC, negative control, ERK, extracellular signal-regulated kinase, Chromosomes, Human, Phosphorylation, Mitogen-Activated Protein Kinase 1, Thy, thymidine, Kinase, chromosome alignment, IP, immunoprecipitation, Biological Sciences, MAP Kinase Kinase Kinases, Cell biology, Dual-Specificity Phosphatases, biological phenomena, cell phenomena, and immunity, hormones, hormone substitutes, and hormone antagonists, Human, Biochemistry & Molecular Biology, CT, C terminus, extracellular signal-regulated kinase 2, 1.1 Normal biological development and functioning, KIM, kinase interaction motif, Mitosis, LAP, localization and affinity purification, Biology, DUSP7, NT, N terminus, PI, phosphatase inhibitor, D7, DUSP7, Chromosomes, DUSP, dual-specificity phosphatase, 03 medical and health sciences, Underpinning research, dual-specificity phosphatase 7 (DUSP7), Dual-specificity phosphatase, medicine, dual-specificity phosphatase 7, Humans, IF, immunofluorescence, Molecular Biology, mitosis, 030102 biochemistry & molecular biology, Chromosome, Cell Biology, medicine.disease, HCT116 Cells, extracellular signal-regulated kinase 2 (ERK2), enzymes and coenzymes (carbohydrates), 030104 developmental biology, Hela Cells, mitogen-activated protein kinases, Chemical Sciences, mitogen-activated protein kinases (MAPK), Mutation, biology.protein, Generic health relevance, OE, overexpression, HeLa Cells

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::119f472aa7d28b25f00860fcbe90d0afTest
http://europepmc.org/articles/PMC8131738Test

9

Conserved proline residues in the coiled coil–OB domain linkers of Rpt proteins facilitate eukaryotic proteasome base assembly

المؤلفون: Michael K. Wong, Mark Hochstrasser, Yanjie Li, Chin Leng Cheng

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Mutant, Sequence Homology, Protein aggregation, Biochemistry, P, pellet, Ubiquitin, BME, β-mercaptoethanol, chaperone, Heat-Shock Proteins, Coiled coil, biology, ARC, AAA+ ATPase forming ring-shaped complexes, Chemistry, OB, oligonucleotide/oligosaccharide-binding, AAA proteins, Cell biology, RP, regulatory particle, IN, induced, RAC, RP assembly chaperone, UN, uninduced, T, total protein, Research Article, Protein Binding, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins, Proline, Ubiquitin-Protein Ligases, PAN, proteasome-activating nucleotidase, protein assembly, AAA+, ATPases associated with diverse cellular activities, Saccharomyces cerevisiae, protein aggregation, 03 medical and health sciences, S, supernatant, Protein Domains, ubiquitin, ATPase, Amino Acid Sequence, PQC, protein quality control, Molecular Biology, 030102 biochemistry & molecular biology, CC, coiled coil, YPD, yeast extract-peptone-dextrose, Cell Biology, CP, core particle, SD, synthetic defined, BCA, bicinchoninic acid, Repressor Proteins, 030104 developmental biology, proteasome, Proteasome, Chaperone (protein), Proteasome assembly, Mutation, biology.protein

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::613d312374996d43ddc183de820a3ad0Test
http://europepmc.org/articles/PMC8134078Test

10

Defining steps in RAVE-catalyzed V-ATPase assembly using purified RAVE and V-ATPase subcomplexes

المؤلفون: Maureen Tarsio, Michael C. Jaskolka, Md. Murad Khan, Patricia M. Kane, Anne M. Smardon

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, assembly, Vacuolar Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins, SEC, size-exclusion chromatography, Endosome, MBP-C, MBP-tagged subunit C, Protein subunit, Mutant, MBP, maltose-binding protein, Vacuole, Saccharomyces cerevisiae, lysosomal acidification, vacuolar ATPase, yeast, Biochemistry, YEPD, 03 medical and health sciences, Maltose-binding protein, chemistry.chemical_compound, YEPD, yeast extract, peptone, 2% dextrose, V-ATPase, BLI, biolayer interferometry, Molecular Biology, RAVE, TBSE, Tris-buffered saline with EDTA, 030102 biochemistry & molecular biology, biology, vacuole, Chemistry, RAVE, Regulator of the H+-ATPase of Vacuoles and Endosomes, regulation, Cell Biology, Yeast, Cell biology, 030104 developmental biology, proton pump, biology.protein, YEP, yeast extract–peptone medium without glucose, Vph1NT, N-terminal domain of Vo subunit Vph1, V-ATPase, vacuolar H+-ATPase, Research Article

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fa2090191f741b721550f4174d1f33aTest
https://pubmed.ncbi.nlm.nih.gov/33895134Test

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